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STRUCTURAL BASIS FOR CHROMOSOME X-LINKED AGAMMAGLOBULINEMIA - A TYROSINE KINASE DISEASE

Vihinen, Mauno LU orcid ; VETRIE, D ; MANIAR, HS ; OCHS, HD ; ZHU, QL ; VORECHOVSKY, I ; WEBSTER, ADB ; NOTARANGELO, LD ; NILSSON, L and SOWADSKI, JM , et al. (1994) In Proceedings of the National Academy of Sciences 91(26). p.12803-12807
Abstract
X-linked agammaglobulinemia (XLA) is a hereditary defect of B-cell differentiation in man caused by deficiency of Bruton tyrosine kinase (BTK). A three-dimensional model for the BTK kinase domain, based on the core structure of cAMP-dependent protein kinase, was used to interpret the structural basis for disease in eight independent point mutations in patients with XLA. As Arg-525 of BTK has been thought to functionally substitute for a critical lysine residue in protein-serine kinases, the mutation Arg-525-->Gln was studied and found to abrogate the tyrosine kinase activity of BTK. All of the eight mutations (Lys-430-->Glu, Arg-520-->Glu, Arg-525-->Gln, Arg-562-->Pro, Ala-582-->Val, Glu-589-->Gly, Gly-594-->Glu,... (More)
X-linked agammaglobulinemia (XLA) is a hereditary defect of B-cell differentiation in man caused by deficiency of Bruton tyrosine kinase (BTK). A three-dimensional model for the BTK kinase domain, based on the core structure of cAMP-dependent protein kinase, was used to interpret the structural basis for disease in eight independent point mutations in patients with XLA. As Arg-525 of BTK has been thought to functionally substitute for a critical lysine residue in protein-serine kinases, the mutation Arg-525-->Gln was studied and found to abrogate the tyrosine kinase activity of BTK. All of the eight mutations (Lys-430-->Glu, Arg-520-->Glu, Arg-525-->Gln, Arg-562-->Pro, Ala-582-->Val, Glu-589-->Gly, Gly-594-->Glu, and Gly-613-->Asp) were located on one face of the BTK kinase domain, indicating structural clustering of functionally important residues. (Less)
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publishing date
type
Contribution to journal
publication status
published
subject
keywords
BRUTON TYROSINE KINASE, BTK, CYTOPLASMIC TYROSINE KINASE, SIGNAL, TRANSDUCTION
in
Proceedings of the National Academy of Sciences
volume
91
issue
26
pages
12803 - 12807
publisher
National Academy of Sciences
external identifiers
  • wos:A1994PY29400093
  • scopus:0028577730
ISSN
1091-6490
DOI
10.1073/pnas.91.26.12803
language
English
LU publication?
no
id
87a72987-2480-472c-97bc-7549d81e6036 (old id 3853307)
date added to LUP
2016-04-01 12:05:39
date last changed
2021-09-19 03:04:48
@article{87a72987-2480-472c-97bc-7549d81e6036,
  abstract     = {{X-linked agammaglobulinemia (XLA) is a hereditary defect of B-cell differentiation in man caused by deficiency of Bruton tyrosine kinase (BTK). A three-dimensional model for the BTK kinase domain, based on the core structure of cAMP-dependent protein kinase, was used to interpret the structural basis for disease in eight independent point mutations in patients with XLA. As Arg-525 of BTK has been thought to functionally substitute for a critical lysine residue in protein-serine kinases, the mutation Arg-525-->Gln was studied and found to abrogate the tyrosine kinase activity of BTK. All of the eight mutations (Lys-430-->Glu, Arg-520-->Glu, Arg-525-->Gln, Arg-562-->Pro, Ala-582-->Val, Glu-589-->Gly, Gly-594-->Glu, and Gly-613-->Asp) were located on one face of the BTK kinase domain, indicating structural clustering of functionally important residues.}},
  author       = {{Vihinen, Mauno and VETRIE, D and MANIAR, HS and OCHS, HD and ZHU, QL and VORECHOVSKY, I and WEBSTER, ADB and NOTARANGELO, LD and NILSSON, L and SOWADSKI, JM and SMITH, CIE}},
  issn         = {{1091-6490}},
  keywords     = {{BRUTON TYROSINE KINASE; BTK; CYTOPLASMIC TYROSINE KINASE; SIGNAL; TRANSDUCTION}},
  language     = {{eng}},
  number       = {{26}},
  pages        = {{12803--12807}},
  publisher    = {{National Academy of Sciences}},
  series       = {{Proceedings of the National Academy of Sciences}},
  title        = {{STRUCTURAL BASIS FOR CHROMOSOME X-LINKED AGAMMAGLOBULINEMIA - A TYROSINE KINASE DISEASE}},
  url          = {{http://dx.doi.org/10.1073/pnas.91.26.12803}},
  doi          = {{10.1073/pnas.91.26.12803}},
  volume       = {{91}},
  year         = {{1994}},
}